ID A0A1R3GZP8_COCAP Unreviewed; 312 AA.
AC A0A1R3GZP8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Phosphatidic acid phosphatase type 2/haloperoxidase {ECO:0000313|EMBL:OMO63608.1};
GN ORFNames=CCACVL1_22384 {ECO:0000313|EMBL:OMO63608.1};
OS Corchorus capsularis (Jute).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO63608.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO63608.1, ECO:0000313|Proteomes:UP000188268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC TISSUE=Whole seedling {ECO:0000313|EMBL:OMO63608.1};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT "Corchorus capsularis genome sequencing.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000256|ARBA:ARBA00008816}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMO63608.1}.
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DR EMBL; AWWV01012913; OMO63608.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3GZP8; -.
DR STRING; 210143.A0A1R3GZP8; -.
DR EnsemblPlants; OMO63608; OMO63608; CCACVL1_22384.
DR Gramene; OMO63608; OMO63608; CCACVL1_22384.
DR OMA; HDLCQVT; -.
DR OrthoDB; 25293at2759; -.
DR Proteomes; UP000188268; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR CDD; cd03390; PAP2_containing_1_like; 1.
DR Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR InterPro; IPR043216; PA_PP_rel.
DR PANTHER; PTHR10165; LIPID PHOSPHATE PHOSPHATASE; 1.
DR PANTHER; PTHR10165:SF183; LIPID PHOSPHATE PHOSPHATASE 2; 1.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000313|EMBL:OMO63608.1};
KW Peroxidase {ECO:0000313|EMBL:OMO63608.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000188268};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 66..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 96..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 226..244
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 98..241
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
FT REGION 289..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 312 AA; 35205 MW; B4259B0D46DB0066 CRC64;
MPEIQLGAHT VRSHGVKVAR THMHDWIILL LLVVIEGILN VIEPFHRFVG EDMMTDLRYP
LKDNTVPFWA VPVIAIIIPF CVILVYYFIR RDVYDLHHAI LGLLFSVLIT GVITDAIKDA
VGRPRPDFFW RCFPDGIGKF HNVTQNVICT GSKSVIKEGH KSFPSGHTSW SFAGLGFLAL
YLSGKIRVFD RRGHVAKLCI VFLPLLIAAL VGISRVDDYW HHWQDVFAGG LLGLTVSSFC
YLQFFPPPYH VDGWGPHAYF QMLAESQNGR PNGQQSELED VYVDSQNGRE LSRANTNDSG
PILDGMDGVR RY
//
